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This interdisciplinary symposium will convene leading experts in adult stem cell research, tissue regeneration and bioengineering to discuss cutting edge research at the intersection of these disciplines, with the overall aim of translating current stem cell knowledge into clinical applications.

Grantsmanship for Students and Postdocs: Pathways to Individual Fellowship

March 20, 2019

Join Science Alliance for “Grantsmanship for Graduate Students and Postdocs” to learn the skills for concise and persuasive writing that is not only vital in academia, but essential for any career path.

This two-day symposium will convene leading experts in cancer immunotherapy to discuss cutting-edge findings in the broad area of combination therapies, including checkpoint inhibitors and cellular therapies. Particular emphasis will be given to the biological mechanisms underlying combination hypotheses, bispecific antibodies and other emerging modalities for delivery of combination therapies, as well as a discussion of the importance of effective clinical trial design.

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Join Dr. Rebecca Nebel from the Society for Women’s Health Research and the Science Alliance to learn more about how to utilize informational interviews for career exploration, networking, and finding the job of your dreams.

Join us at the Academy to learn directly from a PhD hiring manager what they look for in a resume, the best way to communicate technical and transferable skills to a mixed audience, and how to showcase not just what you do but who you are and why an employer should want to hire you.

This panel will highlight the realities of a career change and the opportunities available to scientists who are thinking about a career in teaching. Our guests will discuss what it’s really like to teach in public schools, the shift in culture from a lab to a classroom, and the programs that will help prepare you to get there.

The Junior Academy recruits STEM experts to coach teams of talented, highly motivated students as they compete in science & technology challenges sponsored by industry-leading companies. Students and mentors can participate from anywhere in the world, connecting with one another via Launchpad, our interactive challenge platform.

Available exclusively to our Member community, Member-to-Member Mentoring is a self-directed mentoring program that matches early career scientists and engineers with experienced STEM professionals for advice and coaching.

In this Annals issue, leading scientists and scholars explore the question of meaning through the lens of scientific inquiry, using interdisciplinary approaches to examine the various sources from which we might derive greater insight into the meaning and purpose of human existence.

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For 200 years—since 1817—the Academy has brought together extraordinary people working at the frontiers of discovery. Among the oldest scientific organizations in the United States, it has become not only an enduring cultural institution in New York, but also one of the most significant organizations in the global scientific community.

The unfavorable energetics of the sulfate activating chemistry presents a formidable catalytic challenge to the enzymes charged with timely provision of this essential nutrient. Nature has responded to this challenge with a suite of remarkable molecular inventions, which will be central to our discussion. Once activated, the sulfuryl-moiety can be transferred enzymatically to cellular recipients in reactions that are used widely to regulate metabolism. The first transition-state structure of an enzyme-catalyzed, sulfuryl-transfer reaction was determined recently and will be considered in the context of the enzyme that binds tightly to it – the human estrogen sulfotransferase.

Thiamin pyrophosphate is an essential cofactor in all-living systems and consists of a pyrimidine covalently linked to a thiazole. The biosynthesis of thiamin is complex and different from any of the characterized chemical or biochemical routes to these heterocycles. This lecture will cover the current status of mechanistic and structural studies on the thiazole biosynthetic enzymes as well as related studies on cysteine and thioquinolobactin biosynthesis. The carbon sulfur bond forming steps in each case will be described.

Mycobacterium tuberculosis (M. tb) is the most lethal single infectious agent, accounting for an estimated 3 million deaths per year worldwide. In addition, the number of persons infected with multidrug resistant (MDR) strains of M. tb continues to grow and 79 percent of these cases now show resistance to three or more drugs. These numbers underscore the need for new target identification and antibiotics to address the growing problem of MDR M. tb. To complete its life cycle, M. tb must survive within the nutrient-poor and oxidizing environment of the host macrophage. NO and superoxide are produced in response to M. tb infection and it is likely that the bacterium has a mechanism of protection against these reactive oxidants. Products of the reductive sulfate assimilation pathway, such as the abundant antioxidant mycothiol, are excellent candidates for this function. We are currently investigating the mechanism of APS reductase, the enzyme that catalyzes the first committed step of reductive sulfate assimilation and the role that sulfur-containing metabolites play in the replication and persistence of Mycobacteria. The biosynthetic machinery associated with critical metabolites may offer new targets for anti-tuberculosis therapy.

Estradiol, the principal and most active circulating estrogen, plays an important role in human breast carcinogenesis. Its hormonal activity can be decreased by conjugation to sulfate, which is catalyzed by the homodimeric enzyme estrogen sulfotransferase (EST). A pre-steady state study on EST showed that there is a burst phase (amplitude equals half of the enzyme active sites) in the formation of E2S followed by steady state turnover. Analysis of pre-steady state data and isotope trapping experiments suggests that the ternary central complex equilibrium favors enzyme-bound product formation. In addition, the observation that rate of product Michaelis complex formation was much faster than that of later steps implies that the magnitude of the burst reflects the active enzyme concentration. Taken together, these results demonstrate that EST is a half-of-sites reactivity enzy

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